ArticleNucleic acids research2006
The DNA-protein interaction modes of FEN-1 with gap substrates and their implication in preventing duplication mutations.
Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
25 citing papers in PubMed, 45 citations in OpenAlex.
- USP50 suppresses alternative RecQ helicase use and deleterious DNA2 activity during replication.Nature communications · 2024Article
- PARP1-driven repair of topoisomerase IIIα DNA-protein crosslinks by FEN1.Cell reports · 2024Article
- Processing of matched and mismatched rNMPs in DNA by archaeal ribonucleotide excision repair.iScience · 2023Article
- Precise cut-and-paste DNA insertion using engineered type V-K CRISPR-associated transposases.Nature biotechnology · 2023Article
- A scanning-to-incision switch in TFIIH-XPG induced by DNA damage licenses nucleotide excision repair.Nucleic acids research · 2023Article
- Comprehensive classification of the PIN domain-like superfamily.Nucleic acids research · 2017Article
- Direct observation of DNA threading in flap endonuclease complexes.Nature structural & molecular biology · 2016Article
- The FEN1 E359K germline mutation disrupts the FEN1-WRN interaction and FEN1 GEN activity, causing aneuploidy-associated cancers.Oncogene · 2015Article
- A cryptic targeting signal creates a mitochondrial FEN1 isoform with tailed R-Loop binding properties.PloS one · 2013Article
- Human Fanconi anemia complementation group a protein stimulates the 5' flap endonuclease activity of FEN1.PloS one · 2013Article
- Double strand binding-single strand incision mechanism for human flap endonuclease: implications for the superfamily.Mechanisms of ageing and development · 2012Review
- Functional regulation of FEN1 nuclease and its link to cancer.Nucleic acids research · 2011Review
- FEN1 ensures telomere stability by facilitating replication fork re-initiation.The Journal of biological chemistry · 2010Article
- Dna2 is a structure-specific nuclease, with affinity for 5'-flap intermediates.Nucleic acids research · 2010Article
- The 3'-flap pocket of human flap endonuclease 1 is critical for substrate binding and catalysis.The Journal of biological chemistry · 2009Article
- Human replication factor C stimulates flap endonuclease 1.The Journal of biological chemistry · 2009Article
- PCNA stimulates catalysis by structure-specific nucleases using two distinct mechanisms: substrate targeting and catalytic step.Nucleic acids research · 2008Article
- Physical and functional interaction between human oxidized base-specific DNA glycosylase NEIL1 and flap endonuclease 1.The Journal of biological chemistry · 2008Article
- Removal of oxidative DNA damage via FEN1-dependent long-patch base excision repair in human cell mitochondria.Molecular and cellular biology · 2008Article
- Partial reconstitution of DNA large loop repair with purified proteins from Saccharomyces cerevisiae.Nucleic acids research · 2008Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Flap endonuclease-1 (FEN-1) is a structure-specific nuclease best known for its involvement in RNA primer removal and long-patch base excision repair. This enzyme is known to possess 5'-flap endo- (FEN) and 5'-3' exo- (EXO) nuclease activities. Recently, FEN-1 has been reported to also possess a gap endonuclease (GEN) activity, which is possibly involved in apoptotic DNA fragmentation and the resolution of stalled DNA replication forks. In the current study, we compare the kinetics of these activities to shed light on the aspects of DNA structure and FEN-1 DNA-binding elements that affect substrate cleavage. By using DNA binding deficient mutants of FEN-1, we determine that the GEN activity is analogous to FEN activity in that the single-stranded DNA region of DNA substrates interacts with the clamp region of FEN-1. In addition, we show that the C-terminal extension of human FEN-1 likely interacts with the downstream duplex portion of all substrates. Taken together, a substrate-binding model that explains how FEN-1, which has a single active center, can have seemingly different activities is proposed. Furthermore, based on the evidence that GEN activity in complex with WRN protein cleaves hairpin and internal loop substrates, we suggest that the GEN activity may prevent repeat expansions and duplication mutations.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.